RNase P primarily functions in the 5' maturation of tRNAs. However, several protein subunits of the ribonucleoprotein complex perform noncanonical functions in animals, and recent studies suggest similar functions in plant immunity against viral and fungal pathogens. In rice (Oryza sativa), RNase P subunit 30 (OsRpp30) positively regulates immunity and interacts with the histone deacetylase OsHDT701, a known negative regulator of defense against Magnaporthe oryzae. However, the mechanisms controlling OsRpp30 protein turnover remain unclear. In this study, we identified OsHAG704, a histone acetyltransferase, that acetylates and stabilizes OsRpp30, although OsHAG704-mediated acetylation was not required for OsRpp30 stabilization. Overexpression of OsHAG704 enhanced hydrogen peroxide (H2O2) accumulation and conferred increased resistance to M. oryzae. Additionally, we identified OsBPM2, a BTB/POZ domain-containing E3 ubiquitin ligase, which also interacts with OsRpp30 and promotes its stability, leading to similar enhancements in H2O2 levels and disease resistance. Although OsHAG704 did not physically interact with OsBPM2, both proteins competitively bound to OsRpp30, resulting in mutual interference between their respective regulatory pathways. Together, our findings identify 2 distinct positive regulators of OsRpp30 stability and immunity, highlighting a coordinated mechanism involving HAT- and E3 ligase-mediated stabilization in rice defense against M. oryzae.

The 14-3-3 proteins, a highly conserved class in all eukaryotes, are widely associated with plant growth and stress responses. However, their role in plant immunity and its regulatory mechanisms remains elusive. Here, we show that two homologous rice 14-3-3 proteins, OsGF14f and OsGF14c, function redundantly to enhance rice resistance against Magnaporthe oryzae. The E3 ligase OsPUB20 targets OsGF14f and OsGF14c for ubiquitination and 26S proteasome-mediated degradation, thereby negatively regulating rice immunity. Remarkably, chitin perception activates the receptor-like cytoplasmic kinase OsRLCK185 that phosphorylates OsPUB20 at Thr153, which stabilizes OsGF14f and enhances rice blast resistance. Furthermore, during M. oryzae infection, OsGF14f translocates into the nucleus, where it facilitates the degradation of OsWRKY42, a transcription factor that negatively regulates defense responses. Collectively, our findings reveal a phosphorylation-dependent ubiquitination switch that links cell surface chitin perception to nuclear immune reprogramming during M. oryzae invasion.

Plants deploy intracellular nucleotide-binding leucine-rich repeat (NLR) immune receptors to detect pathogen-secreted virulence effectors and trigger defense responses. NLRs recognize effectors from both adapted and non-adapted pathogens (Dong et al., 2025), either through direct binding or by monitoring effector-induced modifications of host targets (Cesari et al., 2018). Despite these advances, the mechanism by which NLRs evolve new effector-recognition specificities remains a fundamental question in plant immunity. Recently, Gómez de la Cruz et al. (2026) uncovered a novel evolutionary strategy underlying the recognition of the blast fungus effector Pwl2 by the barley NLR MLA3, in which MLA3 acts as a molecular mimic of the effector’s virulence target, the heavy metal-associated protein HIPP43 (Zdrzałek et al., 2024; Were et al., 2025). Importantly, the authors successfully transferred this molecular mimicry interface into the wheat stem rust resistance protein SR50, generating a chimeric NLR receptor with dual pathogen-recognition capabilities. The engineered receptor conferred resistance to both wheat stem rust, caused by Puccinia graminis f. sp. tritici (Pgt), and rice blast disease, caused by Magnaporthe oryzae, in transgenic barley, highlighting the potential of this strategy for developing broad-spectrum and durable disease resistance in crops.

Rosa rugosa is an important aromatic plant and produces flowers that are used in medicine, food, plant essential oils, hydrosols, and other aromatic products. 2-phenylethanol (2-PE) is the main effective substance in the volatile organic compounds of rose fragrance, and its synthesis mechanism in R. rugosa needs to be investigated. We herein present a haplotype-resolved genome of R. rugosa cv. Hanxiang (HX). Pathways mediating the synthesis of scent-related metabolites were deciphered in depth. Allelic imbalances reveal the distinct roles of different haplotyping in shaping the key trait including fragrance during the flower development stages. We deciphered the population structure and genetic composition of rose. Selected and mutated genes in groups of separated aromas including but not limited to one rate-limiting enzymes, primary amine oxidases, is responsible for the high level of 2-PE biosynthesis in R. rugosa, which could provide new genetic resources for enhancing aroma in other species.

Small G proteins, functioning as monomeric GTPases, are critical molecular switches that regulate diverse processes in plants. However, little is known about their protein homeostasis during immune responses. Here, we demonstrate that OsRab11C1, encoding a Rab-type GTPase, is transcriptionally upregulated upon Magnaporthe oryzae infection. Strikingly, loss of OsRab11C1 enhances rice blast resistance, concomitant with increased defense gene expression, MAPK activation, and ROS burst. Mechanistically, we identify the E3 ubiquitin ligase EL5 as an interactor that ubiquitinates and targets OsRab11C1 for degradation via the 26S proteasome. Consistently, EL5 acts upstream of OsRab11C1 and positively regulates rice immunity. Further analysis reveals that OsRab11C1 interacts with and stabilizes mitogen-activated protein kinase kinase OsMKK6, thereby facilitating its autophosphorylation activity. In return, OsMKK6 acts as a negative regulator of rice programmed cell death and immunity. Collectively, our findings unveil a dynamic EL5-OsRab11C1-OsMKK6 signaling module that orchestrates rice immunity against pathogen invasion.

Rice is highly vulnerable to many fungal pathogens that cause major yield losses. Yuan et al. showed that a conserved effector from six fungi targets the susceptibility hub SnRK1β1A. Disrupting this gene confers broad-spectrum resistance, highlighting its potential as a genetic target for improving multipathogen disease resistance in rice.

Abstract Wheat blast, caused by the Magnaporthe oryzae Triticum pathotype (MoT), is a devastating fungal disease that poses a significant global threat to wheat production. Rapid diagnosis is crucial for effective monitoring, containment, and management of this highly transmissible pathogen. In this study, we developed an integrated field-detection kit, named Wheat Blast Rapid Detection Kit (WB-RD kit), which utilizes recombinase polymerase amplification coupled with a nucleic acid lateral flow immunoassay (RPA–NALFIA). The kit is stable for room temperature transportation and achieves a limit of detection as low as 0.1 ng/μL for MoT genomic DNA. The RPA reaction only requires a constant temperature of 39°C for 10 min. The positive result is indicated by the appearance of both a control line and a test line on the lateral flow strip within 5 min. This rapid, precise, user-friendly, and portable method is suitable for both on‑site diagnosis and phytosanitary inspection of seed shipments, providing a practical tool for frontline disease monitoring and quarantine.

Artificial selection of functional genes shapes crops agronomic traits including disease resistance and reproductive development. Recently, Lin et al. (2026) reported that rice nucleotide-binding leucine-rich repeat receptor (NLR) XA48 and its associated transcription factors (TFs) OsVOZ1/2 underwent differential artificial selection upon infection by diverse Xanthomonas oryzae pv. oryzae (Xoo) strains. This asymmetric selection has shaped rice resistance to Xoo and grain yield, uncovering a novel NLR-TF immune module (XA48-VOZs). Here, we discuss the molecular mechanisms of this module, the evolutionary implication of its differential selection, and its potential application, particularly in combination with the pattern-recognition receptor (PRR) XA21 for breeding rice varieties with broad-spectrum resistance to bacterial leaf blight (BLB).

Protein-based biopesticides and biostimulants are critical for the future of sustainable agriculture, yet their utility is severely limited by inefficient delivery into plant cells. Traditional cell-penetrating peptides enable protein uptake but lack the efficiency, systemic activity and scalability required for crop production. Here, we present a potential general solution using a novel engineered membrane translocation domain, MTD4, to enable robust, systemic protein delivery into crops and it is suitable for large-scale application. We first demonstrate that MTD4 enables rapid foliar delivery of a model protein (SEP) and, importantly, facilitates its systemic translocation from lower to upper leaves and from roots to shoots, a key requirement for whole-plant protection. To prove the platform's utility, we fused MTD4 to the harpin protein HrpZ, a known defence elicitor. MTD4-HrpZ delivered into tobacco and tomato plants triggered a potent hypersensitive response and systemic acquired resistance, resulting in significant reductions in disease severity from bacterial and fungal pathogens. Remarkably, the MTD4-HrpZ fusion protein was over five times more effective than HrpZ alone, highlighting MTD4's capacity to dramatically enhance protein efficacy. This work introduces MTD4 as a transformative tool for overcoming protein delivery barriers in plants, paving the way for a new generation of high-potency biotherapeutics that can advance sustainable crop protection and reduce dependence on chemical applications.

INTRODUCTION:Cold constrains the growth and distribution of turfgrasses, which are divided into cool-season and warm-season types with distinct cold adaptation capacities. However, how different grass species evolved distinct strategies to survive the cold remains elusive. OBJECTIVES:This study dissects the functional divergence of DREB1A promoters between the examined cool-season and warm-season turfgrasses and uncovers the underlying transcriptional regulatory mechanisms governing their distinct cold adaptation strategies. METHODS:DREB1As from four grass species were transformed to rice, Arabidopsis WT and cbfs-1 mutant with different promoter-CDS combinations. Binding of ICE1 and ABF to DREB1A promoters was investigated using EMSA, Y1H, and dual-luciferase assays. RESULTS:Functional complementation assays in the cbfs-1 mutant, DREB1A promoters from the two examined warm-season turfgrasses, but not those from the two examined cool-season species, rescued the cold-sensitive phenotype. Consistently, the CdDREB1A promoter from bermudagrass conferred stronger cold tolerance in transgenic Arabidopsis and rice compared to the FaDREB1A promoter from tall fescue. Mechanistically, AtICE1 binds to and activates DREB1A promoters from the examined warm-season turfgrasses, but not those from two cool-season species, in the cbfs-1 mutant background. Moreover, homologous assays confirmed that the two warm-season turfgrass ICE1 proteins directly bind and activate their native DREB1A promoters, whereas the examined cool-season turfgrass ICE1 proteins do not. Furthermore, we identified a novel putative regulatory module, LpABF4-LpDREB1A1, that appears to positively modulates cold signaling in cool-season perennial ryegrass. Overexpression of either LpABF4 or LpDREB1A1 in perennial ryegrass significantly enhanced cold tolerance. CONCLUSION:Our findings support a divergent model wherein the two examined warm-season turfgrasses mainly rely on ICE1-dependent DREB1A induction as part of a cold-avoidance strategy, whereas the other two tested cool-season turfgrasses appear to employ an alternative ABF4-DREB1A1 regulatory module. We could not rule out the possibility that other pathways also modulate the cold stress response in divergent turfgrass species.

SUMMARY Plants deploy a sensor repertoire, usually NLRs, to perceive pathogen effectors and activate executor NLR-triggered immunity. Here we reveal that rice HMA proteins function as sensors detecting the Magnaporthe oryzae MAX effector AvrPigm to trigger broad-spectrum blast resistance mediated by the CNL PigmR. AvrPigm is conserved with multiple copies in blast genomes and targets HMA proteins, facilitating HMA translocation into the cytoplasm. Cryo-EM structure of the HPP04 HMA reveals a filament-like oligomer with ssDNA/RNA bound inside the filament, which display cyclic nucleotide synthase activity to generate 2′,3′-cNMP in a CNL-dependent manner. We further discovered that the LRR domains of the executor CNLs perceive 2′,3′-cNMP to mount immunity. Our study thus establishes an unrecognized immunity mode with a distinct repertoire of sensor receptors that produce signaling molecules that are perceived by the LRR domains of executor NLRs to mediate immunity, shedding new light on the sensor-executor conception and immune activation in plants. Highlights HMA proteins and CNL receptors form a new sensor-executor mode in plant immunity Cryo-EM reveals the filament-like structure of HMA-ssRNA/ssDNA HMA proteins are cyclic nucleotide synthetases to generate 2′,3′-cNMP LRR domains of CNLs perceive 2′,3′-cNMP to mediate immunity

Legumes convert atmospheric nitrogen into ammonium through symbiotic bacteria housed in root nodules, yet the molecular interactions between rhizobial and host proteins inside nodules remain poorly understood. Here we employed AlphaFold3 to construct a cross-kingdom interactome between Medicago truncatula and its symbiont Sinorhizobium meliloti. Screening more than 217,000 protein pairs yielded 7,137 putative interactions, providing a valuable resource for the broader symbiosis community. Within this network, we focused on DEFECTIVE IN NITROGEN FIXATION 2 (DNF2), a host protein required for rhizobial persistence within nodules. We showed that DNF2 localizes to the peribacteroid space and associates with previously uncharacterized secreted rhizobial proteins (SRPs), suggesting it may function as a hub for host-symbiont communication. Notably, knockout of two DNF2-interacting proteins, SRP86 and SRP485, results in white, nitrogen-fixation-deficient nodules with abnormal symbiosomes and elevated expression of senescence-associated genes, closely phenocopying the dnf2 loss-of-function mutant. Together, our findings define a DNF2-SRP molecular framework underlying symbiotic accommodation, and illustrate the potential of AI-guided interactome mapping to uncover molecular mechanisms of plant-microbe interactions with relevance to sustainable agriculture.

Allergic diseases are among the most prevalent conditions globally and are considered one of the three major diseases currently under intensive study and prevention. These diseases have emerged as a significant global public health and safety concern, as well as a focal point in scientific research. An increasing number of individuals are affected by allergic diseases, which can cause a wide range of adverse symptoms and, in severe cases, may lead to fatalities. Despite their prevalence and impact, effective methods for the prevention, diagnosis, and treatment of allergies remain insufficient. In recent years, the incidence of pollen allergy has been increasing, and Chenopodium album stands out as one of the prevalent inhaled pollen allergens during autumn. This plant exhibits a broad distribution, strong environmental adaptability, a large pollen output, and significant allergenicity. Notably, its allergenic potential is particularly pronounced in northern China, especially in regions such as Beijing and Nei Mongol. The yeast surface display system represents an advanced biotechnological platform within the eukaryotic expression system. Equipped with robust post-transcriptional processing and post-translational modification mechanisms, this system facilitates the efficient expression and proper folding of numerous antigens, enabling the formation of functional protein conformations. Consequently, it has emerged as powerful tool for high-throughput screening. In this study, we utilized the yeast surface display method integrated with high-throughput sequencing technology to identify the allergen. Pollen proteins were extracted from Chenopodium album using the acetone precipitation method. Western blot analysis using serum from allergic patients to Chenopodium album revealed allergenic protein molecules ranging from 15 to 95 kD. By combining protein mass spectrometry with transcriptome data of Chenopodium album, we predicted 22 potential allergenic genes. The target fragments were amplified via RT-PCR, and a recombinant plasmid library was constructed through homologous recombination. This library was subsequently transformed into yeast cells (strain EBY100), achieving 89% coverage and successfully displayed on the yeast cell surface after glucose culture and galactose induction. Flow cytometry sorting combined with high throughput sequencing was then employed to identify allergens in Chenopodium album pollen. In conclusion, our findings indicate that: (1) allergenic proteins in Chenopodium album are distributed between 15 and 95 kD; (2) the allergen Che a 4, located at 15 kD, was successfully identified; (3) Che a 4 encodes 133 amino acid residues, has a molecular mass of approximately 14.2 kD, and its open reading frame (ORF) sequence is 402 bp. It belongs to the Profilin family and exhibits 76% similarity with Che a 2. This study represents the pioneering application of the yeast surface display system combined with high-throughput sequencing for identifying plant pollen allergens. It successfully identified a new pollen allergen Che a 4 in Chenopodium album, thereby establishing a foundation for the identification of plant pollen allergens. This work not only provides a scientific basis and technical support for the desensitization treatment of plant allergy patients but also enriches the epidemiological data on local allergies.

High soil salinity has become a key factor affecting the yield and quality of alfalfa. Calmodulin 1 (CaM1) gene is involved in salinity stress signal transduction, which plays a positive or negative role in regulating plant salinity tolerance. Nevertheless, the specific function of MsCaM1 in alfalfa remains unknown. This study showed that the MsCaM1 gene contains a complete open reading frame of 450 bp, encoding a protein of 149 amino acids. Subcellular localization analysis revealed that the MsCaM1 protein is located to the nucleus. Meanwhile, the expression of MsCaM1 gene showed increased trend by salinity treatment in leaves of salinity tolerance variety GN5. The heterologous expression of MsCaM1 in Arabidopsis resulted in increased germination energy, germination percentage, plant height, and shoot fresh weight compared with wild-type. Moreover, the shoots of transgenic Arabidopsis plants under NaCl treatment displayed better growth compared to wild-type plants. In transgenic Arabidopsis, the MDA content significantly decreased by NaCl-treated, while the SOD activity remained unchanged, contrasting with the wild-type, where MDA content unchanged and SOD activity decreased. Moreover, the transgenic Arabidopsis plants have lower O2− level under salinity stress compared to wild-type. Furthermore, MsCaM1 expression significantly affected the expression of the AtCaM1 genes. These results indicate that MsCaM1 may act as a positive regulator of growth and salt tolerance in Arabidopsis. These findings could contribute to the understanding of the role of MsCaM1 in alfalfa.

Plant surface immune receptors are tightly controlled to maintain homeostasis and prevent overactivation. However, the mechanisms coordinating the balance remain largely unknown. The monocot-specific receptor-like kinase SDS2 regulates cell death and immunity in rice. Here, we identify Thr671, a conserved phospho-switch in RD-type Ser/Thr kinases across kingdoms, as the central node that orchestrates both immune activation and turnover of SDS2. Autophosphorylation of Thr671 initiates signaling but also primes SDS2 for ubiquitination and degradation by the E3 ligase SPL11. This degradation is antagonized by the phosphatase SIPP1, which stabilizes SDS2 through Thr671 dephosphorylation to promote immunity. Strikingly, a second phosphatase, SIPP2, displaces SIPP1 from SDS2 via competitive binding, thereby enabling SPL11-dependent SDS2 degradation and ensuring timely immune attenuation. Thus, the SIPP1-SPL11-SIPP2 module establishes a dynamic equilibrium essential for SDS2 homeostasis, providing new insights into the sophisticated regulation of surface receptors.

Pathogens commonly secrete effectors into host cells to facilitate invasion. In the host ubiquitin-proteasome system (UPS), E3 ubiquitin ligases often target pathogen effectors for degradation, thereby enhancing immune responses. In turn, pathogen effectors frequently disrupt E3 ligase function to promote virulence. However, it remains largely unclear whether pathogen effectors also interfere with other enzymes of the UPS, such as E2 ubiquitin-conjugating enzymes. In this study, we identified a conserved effector, MoCE1, that is essential for the pathogenicity of Magnaporthe oryzae. MoCE1 is secreted into rice cells, where it interacts with the rice E3 ligase OsRING10 and the E2 enzyme OsUBC11. Upon M. oryzae infection, OsRING10 and OsUBC11 act synergistically to degrade MoCE1 through K48-linked polyubiquitination. Overexpression of either OsRING10 or OsUBC11 enhances resistance to M. oryzae. To counteract this defence, MoCE1 inhibits the enzymatic activity of OsUBC11. Collectively, these findings reveal a nuanced mechanism in which a pathogen effector, regulated by a host E2-E3 pair, disrupts E2 function to escape UPS-mediated immunity in plants.

Abstract 14‐3‐3 proteins are a highly conserved family of regulatory proteins that orchestrate diverse cellular processes through interactions with phosphorylated target proteins. Recent studies have identified rice 14‐3‐3 proteins as pivotal regulators of plant immunity, revealing both positive and negative roles in defense against the blast fungus Magnaporthe oryzae . OsGF14f and OsGF14c function as positive regulators by linking chitin perception to nuclear transcriptional reprogramming through an OsRLCK185–OsPUB20 signaling cascade, ultimately promoting the degradation of the defense suppressor OsWRKY42. In contrast, OsGF14d acts as a negative regulator of immunity by facilitating the oxidative activation of the transcription factor BSR‐D1, thereby enhancing the expression of hydrogen peroxide‐scavenging genes. Together, these findings establish 14‐3‐3 proteins as versatile signaling hubs that integrate phosphorylation, ubiquitination, redox regulation, and transcriptional control to fine‐tune plant immune responses. This article summarizes these recent advances and discusses future research directions for elucidating the diverse functions of 14‐3‐3 proteins in rice immunity, as well as their potential applications in engineering broad‐spectrum and durable disease resistance in crops.

Centromeres are essential for centromere-specific histone H3 (CENH3) recruitment and kinetochore assembly, ensuring accurate chromosome segregation and maintaining genome stability in plants. Although extensively studied in model species, the structural organization of centromeres in nonmodel plants, such as fruit trees, remains poorly explored. Our previous study revealed that jujube centromeres lack the typical tandem repeat (TR)-rich structure, complicating their precise identification. In this study, we updated the genome assembly of jujube (Ziziphus jujuba Mill. 'Dongzao') to a haplotype-resolved T2T version, enabling accurate mapping and comparison of centromeres between haplotypes using CENH3 ChIP-seq. These centromeres, ranging from 0.75 to 1.40 Mb, are largely conserved between haplotypes, except for a localized inversion on chromosome 10. Unlike the TR-rich centromeres found in many plant species, jujube centromeres are predominantly composed of Gypsy-type long-terminal repeat retrotransposons (LTR-RTs). Among these, we identified a centromere-enriched LTR family, centromeric retrotransposons of jujube (CRJ), which is particularly abundant in terminal LTRs compared to the internal transposon regions. Comparative analysis across plant species revealed that centromeric retrotransposons primarily fall into three subfamilies-CRM, Tekay, and Athila-highlighting strong subfamily specificity. Notably, early insertions of CRJ-derived LTR segments contributed to the formation of TR-like structures, suggesting a mechanistic link between transposable elements and the evolution of centromeric tandem repeats. This work provides the first in-depth characterization of a TE-dominated centromere architecture in a fruit tree, offering new insights into the diversity and evolution of plant centromeres.

Covalent small molecule drugs have emerged as a crucial support in precision therapy due to their high selectivity and robust potency. Covalent DNA-encoded chemical library (CoDEL) technology is an advanced platform for covalent drug discovery. However, the application of CoDELs is constrained by a single-residue focus and limited warhead diversity. Here we report a method to identify residue-selective inhibitors using CoDELs with diverse warheads targeting multiple distinct residues. We systematically evaluated the reactivity of 17 warheads with 9 nucleophilic amino acids of FGFR2 and then constructed CoDELs comprising 24.8 million compounds. These CoDELs enabled the identification of active covalent inhibitors targeting cysteine, lysine, arginine, or glutamic acid. The lysine-targeting inhibitor engaged a novel reactive site. The arginine-targeting inhibitor demonstrated subtype selectivity and overcame drug resistance. The glutamic acid-targeting inhibitor validated the druggability of this unconventional covalent residue site. These findings suggest that our work could potentially expand the target space of covalent drugs and promote precision therapy by harnessing the power of the CoDELs.

Supplementary Figure S1, S2, S3